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RN185_PONAB
ID   RN185_PONAB             Reviewed;         192 AA.
AC   Q5RFK9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF185;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96GF1};
DE   AltName: Full=RING finger protein 185;
GN   Name=RNF185;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that regulates selective
CC       mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination
CC       of BNIP1. Acts in the endoplasmic reticulum (ER)-associated degradation
CC       (ERAD) pathway, which targets misfolded proteins that accumulate in the
CC       endoplasmic reticulum (ER) for ubiquitination and subsequent
CC       proteasome-mediated degradation. Protects cells from ER stress-induced
CC       apoptosis. Responsible for the cotranslational ubiquitination and
CC       degradation of CFTR in the ERAD pathway. Also acts as a regulator of
CC       the innate antiviral response by catalyzing 'Lys-27'-linked
CC       polyubiquitination of CGAS, thereby promoting CGAS cyclic GMP-AMP
CC       synthase activity. Preferentially associates with the E2 enzymes UBE2J1
CC       and UBE2J2. {ECO:0000250|UniProtKB:Q96GF1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q96GF1};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q96GF1}.
CC   -!- SUBUNIT: Interacts with ATG5 and BNIP1. {ECO:0000250|UniProtKB:Q96GF1}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q96GF1}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q96GF1}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q96GF1}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q96GF1}.
CC   -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC       ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q96GF1}.
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DR   EMBL; CR857146; CAH89448.1; -; mRNA.
DR   RefSeq; NP_001124620.1; NM_001131148.1.
DR   AlphaFoldDB; Q5RFK9; -.
DR   SMR; Q5RFK9; -.
DR   STRING; 9601.ENSPPYP00000013084; -.
DR   Ensembl; ENSPPYT00000013617; ENSPPYP00000013084; ENSPPYG00000011729.
DR   GeneID; 100171457; -.
DR   KEGG; pon:100171457; -.
DR   CTD; 91445; -.
DR   eggNOG; KOG0823; Eukaryota.
DR   GeneTree; ENSGT00390000014107; -.
DR   HOGENOM; CLU_055198_2_2_1; -.
DR   InParanoid; Q5RFK9; -.
DR   OMA; RTFECNI; -.
DR   OrthoDB; 1510545at2759; -.
DR   TreeFam; TF317334; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Chromosome 22.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IEA:Ensembl.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:1904294; P:positive regulation of ERAD pathway; ISS:UniProtKB.
DR   GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR   GO; GO:0044314; P:protein K27-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR045103; RNF5/RNF185-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12313; PTHR12313; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Endoplasmic reticulum; Immunity; Innate immunity; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..192
FT                   /note="E3 ubiquitin-protein ligase RNF185"
FT                   /id="PRO_0000247522"
FT   TOPO_DOM        1..130
FT                   /note="Cytoplasmic"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        152..171
FT                   /note="Mitochondrial intermembrane"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         39..80
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          29..80
FT                   /note="Required for ubiquitin ligase activity and
FT                   protection against ER stress-induced cell death"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GF1"
FT   REGION          90..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   192 AA;  20475 MW;  F833239856754D53 CRC64;
     MASKGPSASS SPENSSAGGP SGSSNGAGES GGQDSTFECN ICLDTAKDAV ISLCGHLFCW
     PCLHQWLETR PNRQVCPVCK AGISRDKVIP LYGRGSTGQQ DPREKTPPRP QGQRPEPENR
     GGFQGFGFGD GGFQMSFGIG AFPFGIFATA FNINDGRPPP AVPGTPQYVD EQFLSRLFLF
     VALVIMFWLL IA
 
 
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